Prion formation by a yeast GLFG nucleoporin
Author(s)Halfmann, Randal Arthur; Wright, Jessica R.; Alberti, Simon; Lindquist, Susan; Rexach, Michael
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The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic elements in an entirely protein-based system of inheritance. The nuclear pore complex (NPC) contains multiple Q/N-rich proteins whose self-assembly has also been proposed to underlie structural and functional properties of the NPC. Here we show that an essential sequence feature of these proteins—repeating GLFG motifs—strongly promotes their self-assembly into amyloids with characteristics of prions. Furthermore, we demonstrate that Nup100 can form bona fide prions, thus establishing a previously undiscovered ability of yeast GLFG nucleoporins to adopt this conformational state in vivo.
DepartmentMassachusetts Institute of Technology. Department of Biology; Whitehead Institute for Biomedical Research
Halfmann, Randal, Jessica R. Wright, Simon Alberti, Susan Lindquist, and Michael Rexach. “Prion formation by a yeast GLFG nucleoporin.” Prion 6, no. 4 (September 1, 2012): 391-399.
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